BIOL 112 |
| Collagen is the most abundant protein in animals. The post-translational modification of collagen by the enzyme prolyl 4-hydroxylase increases markedly the conformational stability of the collagen triple helix. We have discovered that a previously unappreciated force—stereoelectronic effects—is responsible for this increased stability. By exploiting these stereoelectronic effects (e.g., the gauche effect and n→π* interaction), reciprocal steric effects, and molecular self-assembly, we are creating synthetic collagens of unprecedented stability and length for applications in biotechnology and biomedicine. In addition, we have shown that these stereoelectronic effects stabilize polyproline type II helices and the trans isomer of peptide bonds, and thus have a widespread impact on the structure and function of proteins. (For a recent review, see: Protein Sci. 2006, 15, 1219–1225.)
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Murray Goodman Award Symposium
2:00 PM-4:40 PM, Monday, August 20, 2007 BCEC -- 109 A/B, Oral
Division of Biological Chemistry |
